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Journal Abstract Search

181 related items for PubMed ID: 18245105

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  • 2. Oxidative folding pathway of onconase, a ribonuclease homologue: insight into oxidative folding mechanisms from a study of two homologues.
    Gahl RF, Scheraga HA.
    Biochemistry; 2009 Mar 31; 48(12):2740-51. PubMed ID: 19309163
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  • 4. Characterization of the fast-forming intermediate, des [30-75], in the reductive unfolding of onconase.
    Xu G, Narayan M, Welker E, Scheraga HA.
    Biochemistry; 2004 Mar 23; 43(11):3246-54. PubMed ID: 15023075
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  • 7. Comparison of local and global stability of an analogue of a disulfide-folding intermediate with those of the wild-type protein in bovine pancreatic ribonuclease A: identification of specific regions of stable structure along the oxidative folding pathway.
    Laity JH, Montelione GT, Scheraga HA.
    Biochemistry; 1999 Dec 14; 38(50):16432-42. PubMed ID: 10600104
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  • 8. A new method for rapid characterization of the folding pathways of multidisulfide-containing proteins.
    Welker E, Hathaway L, Scheraga HA.
    J Am Chem Soc; 2004 Mar 31; 126(12):3720-1. PubMed ID: 15038718
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  • 11. Development of a novel method to populate native disulfide-bonded intermediates for structural characterization of proteins: implications for the mechanism of oxidative folding of RNase A.
    English BP, Welker E, Narayan M, Scheraga HA.
    J Am Chem Soc; 2002 May 08; 124(18):4995-9. PubMed ID: 11982363
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  • 13. Impact of an easily reducible disulfide bond on the oxidative folding rate of multi-disulfide-containing proteins.
    Leung HJ, Xu G, Narayan M, Scheraga HA.
    J Pept Res; 2005 Jan 08; 65(1):47-54. PubMed ID: 15686534
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  • 14. Role of the [65-72] disulfide bond in oxidative folding of bovine pancreatic ribonuclease A.
    Shin HC, Narayan M, Song MC, Scheraga HA.
    Biochemistry; 2003 Oct 07; 42(39):11514-9. PubMed ID: 14516203
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  • 15. NMR structural analysis of an analog of an intermediate formed in the rate-determining step of one pathway in the oxidative folding of bovine pancreatic ribonuclease A: automated analysis of 1H, 13C, and 15N resonance assignments for wild-type and [C65S, C72S] mutant forms.
    Shimotakahara S, Rios CB, Laity JH, Zimmerman DE, Scheraga HA, Montelione GT.
    Biochemistry; 1997 Jun 10; 36(23):6915-29. PubMed ID: 9188686
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  • 16. Contribution of structural peculiarities of onconase to its high stability and folding kinetics.
    Arnold U, Schulenburg C, Schmidt D, Ulbrich-Hofmann R.
    Biochemistry; 2006 Mar 21; 45(11):3580-7. PubMed ID: 16533040
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  • 17. Oxidative folding of proteins.
    Narayan M, Welker E, Wedemeyer WJ, Scheraga HA.
    Acc Chem Res; 2000 Nov 21; 33(11):805-12. PubMed ID: 11087317
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  • 18. Effect of glutaredoxin and protein disulfide isomerase on the glutathione-dependent folding of ribonuclease A.
    Ruoppolo M, Lundström-Ljung J, Talamo F, Pucci P, Marino G.
    Biochemistry; 1997 Oct 07; 36(40):12259-67. PubMed ID: 9315864
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  • 19. Simultaneous characterization of the reductive unfolding pathways of RNase B isoforms by top-down mass spectrometry.
    Xu G, Zhai H, Narayan M, McLafferty FW, Scheraga HA.
    Chem Biol; 2004 Apr 07; 11(4):517-24. PubMed ID: 15123246
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  • 20. The folding pathway of onconase is directed by a conserved intermediate.
    Schulenburg C, Löw C, Weininger U, Mrestani-Klaus C, Hofmann H, Balbach J, Ulbrich-Hofmann R, Arnold U.
    Biochemistry; 2009 Sep 08; 48(35):8449-57. PubMed ID: 19655705
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